Aggresome formation in neuropathy models based on peripheral myelin protein 22 mutations

Neurobiology of Disease

Volumn 10, Issue 2, 2002, Pages 109-118

  Ryan, Mary C ^a   Shooter, Eric M ^a   Notterpek, Lucia ^b  

^a STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF FLORIDA COLLEGE OF MEDICINE   (United States)

Author keywords

Aggresomes; PMP22; Protein degradation; Schwann cells; Trembler mice; Ubiquitin proteasome pathway

Indexed keywords

ALPHA CRYSTALLIN; CHAPERONE; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; MYELIN PROTEIN; PERIPHERAL MYELIN PROTEIN 22; UNCLASSIFIED DRUG;

ANIMAL CELL; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DEMYELINATING NEUROPATHY; DISEASE MODEL; GENE MUTATION; GENE OVEREXPRESSION; HOMOZYGOTE; MICROTUBULE; MOUSE; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DEGRADATION; RAT; SCHWANN CELL; SIGNAL TRANSDUCTION; WILD TYPE;

EID: 0036070537     PISSN: 09699961     EISSN: None     Source Type: Journal    
DOI: 10.1006/nbdi.2002.0500     Document Type: Article

References (31)

1. Chaperone activity of alpha B-crystallin suppresses tubulin aggregation through complex formation
2. Impairment of the ubiquitin-proteasome system by protein aggregation
3. Alpha B-crystallin in cardiac tissue. Association with actin and desmin filaments
4. Lactacystin and clasto-lactacystin beta-lactone modify multiple proteasome beta-subunits and inhibit intracellular protein degradation and major histocompatibility complex class I antigen presentation
5. Overloaded endoplasmic reticulum-Golgi compartments, a possible pathomechanism of peripheral neuropathies caused by mutations of the peripheral myelin protein PMP22
6. The receptor for ciliary neurotrophic factor
7. Setting the standards: Quality control in the secretory pathway
8. Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera
9. Molecular chaperones in cellular protein folding
10. Molecular chaperone functions of heat-shock proteins
11. Alpha-crystallin can function as a molecular chaperone
12. Aggresomes: A cellular response to misfolded proteins
13. Aggresomes, inclusion bodies and protein aggregation
14. Charcot-Marie-Tooth peripheral neuropathies and related disorders
15. Aberrant protein trafficking in Trembler suggests a disease mechanism for hereditary human peripheral neuropathies
16. Many facets of the peripheral myelin protein PMP22 in myelination and disease
17. Upregulation of the endosomal-lysosomal pathway in the Trembler-J neuropathy
18. PMP22 accumulation in aggresomes: Implications for CMT1A pathology
19. Neurons promote the translocation of peripheral myelin protein 22 into myelin
20. Pathology and biology of the Lewy body
21. Expression of alpha B-crystallin in Alzheimer's disease
22. Role of the peripheral myelin protein 22 N-linked glycan in oligomer stability
23. Mutations in peripheral myelin protein 22 result in defective trafficking through mechanisms, which may be common to diseases involving tetraspan membrane proteins
24. Misfolding of membrane proteins in health and disease: The lady or the tiger?
25. Characterization of a novel peripheral nervous system myelin protein (PMP-22/SR13)
26. trkB encodes a functional receptor for brain-derived neurotrophic factor and neurotrophin-3 but not nerve growth factor
27. A leucine-to-proline mutation in the putative first transmembrane domain of the 22-kDa peripheral myelin protein in the Trembler-J mouse
28. Trembler mouse carries a point mutation in a myelin gene
29. Transport of Trembler-J mutant peripheral myelin protein 22 is blocked in the intermediate compartment and affects the transport of the wt protein by direct interaction
30. Differential aggregation of the Trembler and Trembler J mutants of peripheral myelin protein 22
31. EBV-induced expression and HLA-DR-restricted presentation by human B cells of alpha B-crystallin, a candidate autoantigen in multiple sclerosis